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1.
Diabetes Res Clin Pract ; 106(3): 605-10, 2014 Dec.
Article in English | MEDLINE | ID: mdl-25312871

ABSTRACT

AIMS: Resting energy expenditure (REE) plays a critical role in the regulation of body weight, with important implications in type 2 diabetes (T2D). However, the relationships between REE and T2D have not been extensively evaluated. We compared REE in persons with diabetes and in persons without diabetes. We also investigated the acute effect of insulin on REE and venous lactate, the latter an indirect measure of neoglucogenetic activity. METHODS: REE was measured using indirect calorimetry in 14 newly diagnosed, untreated T2D adults and in 14 non-diabetic age-, gender- and body mass index-matched persons. The REE and lactate venous concentrations were also measured in a subgroup of 5 T2D patients in the hour following an IV insulin bolus. RESULTS: The REE normalized for fat-free mass (FFM) was significantly higher in T2D patients than in the group without diabetes (mean ± SD: 27.6 ± 1.9 vs. 25.8 ± 1.9 kcal/kg-FFM·24h; P=0.02). REE normalized for FFM was correlated with fasting plasma glucose concentration (r=0.51; P=0.005). Following the insulin venous bolus REE (0': 2,048 ± 242; 10': 1,804 ± 228; 20': 1,684 ± 230; 30': 1,634 ± 212; 45': 1,594 ± 179; 60': 1,625 ± 197 kcal/24h; P<0.001) and both glucose (P<0.001) and lactate (P<0.001) concentrations progressively declined in the ensuing hour. CONCLUSIONS: Patients with diabetes have a higher energy expenditure, likely a consequence of higher gluconeogenetic activity. This study may contribute to recognizing the nature of body weight reduction that occurs in concomitance with poorly controlled diabetes, and of body weight gain as commonly observed when hypoglycemic treatment is started.


Subject(s)
Body Weight/physiology , Diabetes Mellitus, Type 2/metabolism , Energy Intake/physiology , Energy Metabolism/physiology , Insulin/administration & dosage , Rest/physiology , Adult , Aged , Blood Glucose/drug effects , Blood Glucose/metabolism , Body Mass Index , Calorimetry, Indirect , Diabetes Mellitus, Type 2/drug therapy , Diabetes Mellitus, Type 2/physiopathology , Female , Follow-Up Studies , Humans , Hypoglycemic Agents/administration & dosage , Male , Middle Aged
2.
Endocrinology ; 148(1): 252-7, 2007 Jan.
Article in English | MEDLINE | ID: mdl-17053029

ABSTRACT

We previously identified a cold shock domain (CSD)-containing protein (PIPPin), expressed at high level in brain cells. PIPPin has the potential to undergo different posttranslational modifications and might be a good candidate to regulate the synthesis of specific proteins in response to extracellular stimuli. Here we report the effects of T(3) on PIPPin expression in developing rat brain. We found that a significant difference among euthyroid and hypothyroid newborn rats concerns sumoylation of nuclear PIPPin, which is abolished by hypothyroidism. Moreover, T(3) dependence of PIPPin sumoylation has been confirmed in cortical neurons purified from brain cortices and cultured in a chemically defined medium (Maat medium), with or without T(3). We also report that about one half of unmodified as well as all the sumoylated form of PIPPin could be extracted from nuclei with HCl, together with histones. Moreover, this HCl-soluble fraction remains in the nucleus even after treatment with 0.6 M KCl, thus suggesting strong interaction of PIPPin with nuclear structures and perhaps chromatin.


Subject(s)
Cerebral Cortex/embryology , Hypothyroidism/physiopathology , Nerve Tissue Proteins/metabolism , RNA-Binding Proteins/metabolism , SUMO-1 Protein/metabolism , Triiodothyronine/pharmacology , Animals , Animals, Newborn , Antithyroid Agents/pharmacology , Cell Nucleus/metabolism , Cells, Cultured , Cerebral Cortex/drug effects , Cerebral Cortex/metabolism , Female , Hypothyroidism/chemically induced , Hypothyroidism/pathology , Nerve Tissue Proteins/chemistry , Neurons/drug effects , Neurons/metabolism , Pregnancy , Prenatal Exposure Delayed Effects , Propylthiouracil/pharmacology , Protein Structure, Tertiary , RNA-Binding Proteins/chemistry , Rabbits , Rats , Rats, Wistar
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